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Q15025 (TNIP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 131. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
TNFAIP3-interacting protein 1
Alternative name(s):
A20-binding inhibitor of NF-kappa-B activation 1
Short name=ABIN-1
HIV-1 Nef-interacting protein
Nef-associated factor 1
Short name=Naf1
Nip40-1
Virion-associated nuclear shuttling protein
Short name=VAN
Short name=hVAN
Gene names
Name:TNIP1
Synonyms:KIAA0113, NAF1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length636 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Interacts with zinc finger protein A20/TNFAIP3 and inhibits TNF-induced NF-kappa-B-dependent gene expression by interfering with an RIP- or TRAF2-mediated transactivation signal; however, binding to A20/TNFAIP3 seems not to be required for this function By similarity. Inhibits NF-kappa-B activation by regulating A20/TNFAIP3-mediated deubiquitination of IKBKG; proposed to link A20/TNFAIP3 to ubiquitinated IKBKG. Involved in regulation of EGF-induced ERK1/ERK2 signaling pathway; blocks MAPK3/MAPK1 nuclear translocation and MAPK1-dependent transcricption. Increases cell surface CD4(T4) antigen expression. Involved in the anti-inflammatory response of macrophages and positively regulates TLR-induced activation of CEBPB. Involved in the prevention of autoimmunity; this function implicates binding to polyubiquitin. Involved in leukocyte integrin activation during inflammation; this function is mediated by association with SELPLG and dependent on phosohorylation by SRC-family kinases. Interacts with HIV-1 matrix protein and is packaged into virions and overexpression can inhibit viral replication. May regulate matrix nuclear localization, both nuclear import of PIC (Preintegration complex) and export of GAG polyprotein and viral genomic RNA during virion production. In case of infection, promotes association of IKBKG with Shigella flexneri E3 ubiquitin-protein ligase ipah9.8 p which in turn promotes polyubiquitination of IKBKG leading to its proteasome-dependent degradation and thus is perturbing NF-kappa-B activation during bacterial infection. Ref.12 Ref.13 Ref.15 Ref.19

Subunit structure

Interacts with TNFAIP3 and IKBKG; facilitates TNFAIP3-mediated de-ubiquitination of NEMO/IKBKG. Interacts with HIV-1 matrix protein. Interacts with Shigella flexneri ipah9.8; the interaction promotes polyubiquitination of IKBKG. Interacts with polyubiquitin. Interacts with MAPK1, SELPLG and PIK3CD. Interacts with IKBKG (polyubiquitinated). Interacts with IRAK1 (polyubiquitinated). Interacts with MYD88; the interaction is indicative for participation in an activated TLR-signaling complex By similarity. Ref.12 Ref.13 Ref.15 Ref.19

Subcellular location

Cytoplasm. Nucleus. Note: Shuttles between the nucleus and cytoplasm in a CRM1-dependent manner.

Tissue specificity

Ubiquitous. Strongly expressed in peripheral blood lymphocytes, spleen and skeletal muscle, and is weakly expressed in the brain.

Post-translational modification

Phosphorylation at Tyr-552 by SRC-family kinases recruits phosphoinositide-3-kinase (PI3K) PIK3CD:p85 heterodimer which results in integrin activation and leukocyte adhesion to activated endothelium during inflammation.

Sequence caution

The sequence AAB41438.1 differs from that shown. Reason: Frameshift at positions 152 and 154.

Ontologies

Keywords
   Biological processInflammatory response
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processMyD88-dependent toll-like receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

defense response

Traceable author statement Ref.1. Source: ProtInc

glycoprotein biosynthetic process

Inferred from direct assay Ref.1. Source: UniProtKB

inflammatory response

Inferred from electronic annotation. Source: UniProtKB-KW

leukocyte cell-cell adhesion

Inferred from mutant phenotype Ref.15. Source: UniProtKB

modulation by symbiont of host I-kappaB kinase/NF-kappaB cascade

Inferred from direct assay Ref.19. Source: UniProtKB

negative regulation of ERK1 and ERK2 cascade

Inferred from direct assay Ref.12. Source: UniProtKB

negative regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from direct assay Ref.13. Source: UniProtKB

negative regulation of viral genome replication

Traceable author statement Ref.1. Source: UniProtKB

positive regulation of inflammatory response

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from sequence or structural similarity. Source: UniProtKB

translation

Traceable author statement Ref.1. Source: ProtInc

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

intracellular

Traceable author statement Ref.1. Source: UniProtKB

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionmitogen-activated protein kinase binding

Inferred from direct assay Ref.12. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q15025-1)

Also known as: Alpha;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q15025-2)

Also known as: Beta;

The sequence of this isoform differs from the canonical sequence as follows:
     627-636: SPKNDREGPQ → PADLRLPRN
Note: No experimental confirmation available.
Isoform 3 (identifier: Q15025-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-53: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 636636TNFAIP3-interacting protein 1
PRO_0000096691

Regions

Region94 – 412319Interacts with Nef
Region351 – 36717Interaction with Shigella flexneri ipah9.8
Region431 – 588158Required for inhibitory activity of TNF-induced NF-kappa-B activation By similarity
Region452 – 51059Ubiquitin-binding domain (UBD)
Coiled coil20 – 7354 Potential
Coiled coil196 – 25863 Potential
Coiled coil294 – 535242 Potential
Motif524 – 5307Nuclear localization signal Potential
Compositional bias539 – 63698Pro-rich

Amino acid modifications

Modified residue4031Phosphoserine Ref.14 Ref.16 Ref.20
Modified residue4381Phosphothreonine Ref.18
Modified residue4421Phosphoserine Ref.20
Modified residue5521Phosphotyrosine Ref.15

Natural variations

Alternative sequence1 – 5353Missing in isoform 3.
VSP_045296
Alternative sequence627 – 63610SPKNDREGPQ → PADLRLPRN in isoform 2.
VSP_003913
Natural variant1031P → S.
Corresponds to variant rs2303018 [ dbSNP | Ensembl ].
VAR_051453
Natural variant1461A → V.
Corresponds to variant rs2233289 [ dbSNP | Ensembl ].
VAR_051454
Natural variant1511P → A.
Corresponds to variant rs2233290 [ dbSNP | Ensembl ].
VAR_051455
Natural variant2331R → Q.
Corresponds to variant rs2233292 [ dbSNP | Ensembl ].
VAR_051456
Natural variant2601A → V.
Corresponds to variant rs2233295 [ dbSNP | Ensembl ].
VAR_051457
Natural variant2631R → W in patients with gastrointestinal diffuse large cell lymphoma. Ref.23
Corresponds to variant rs117663772 [ dbSNP | Ensembl ].
VAR_067965
Natural variant2861T → M in patients with gastrointestinal diffuse large cell lymphoma; somatic mutation. Ref.23
Corresponds to variant rs185683917 [ dbSNP | Ensembl ].
VAR_067966
Natural variant3741I → T in patients with gastrointestinal diffuse large cell lymphoma. Ref.23
VAR_067967
Natural variant4761E → K in patients with gastrointestinal diffuse large cell lymphoma; somatic mutation; loss of inhibitory activity on CARD11- and TNF-induced NF-kappa-B activation. Ref.23
VAR_067968

Experimental info

Mutagenesis4721D → N: Abolishes binding to polyubiquitin ('K-63'-linked and linear). Ref.19 Ref.22
Mutagenesis5521Y → F: Abolishes interaction with PI3K p85 regulatory subunit and abolishes interaction between SELPLG and PI3K p85 regulatory subunit. Ref.15 Ref.19
Sequence conflict1481G → D in AAH12133. Ref.9
Sequence conflict1781G → S in BAH13185. Ref.5
Sequence conflict2991A → P in AAG42154. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Alpha) [UniParc].

Last modified August 1, 1999. Version 2.
Checksum: D81B96BEAD50D871

FASTA63671,864
        10         20         30         40         50         60 
MEGRGPYRIY DPGGSVPSGE ASAAFERLVK ENSRLKEKMQ GIKMLGELLE ESQMEATRLR 

        70         80         90        100        110        120 
QKAEELVKDN ELLPPPSPSL GSFDPLAELT GKDSNVTASP TAPACPSDKP APVQKPPSSG 

       130        140        150        160        170        180 
TSSEFEVVTP EEQNSPESSS HANAMALGPL PREDGNLMLH LQRLETTLSV CAEEPDHGQL 

       190        200        210        220        230        240 
FTHLGRMALE FNRLASKVHK NEQRTSILQT LCEQLRKENE ALKAKLDKGL EQRDQAAERL 

       250        260        270        280        290        300 
REENLELKKL LMSNGNKEGA SGRPGSPKME GTGKKAVAGQ QQASVTAGKV PEVVALGAAE 

       310        320        330        340        350        360 
KKVKMLEQQR SELLEVNKQW DQHFRSMKQQ YEQKITELRQ KLADLQKQVT DLEAEREQKQ 

       370        380        390        400        410        420 
RDFDRKLLLA KSKIEMEETD KEQLTAEAKE LRQKVKYLQD QLSPLTRQRE YQEKEIQRLN 

       430        440        450        460        470        480 
KALEEALSIQ TPPSSPPTAF GSPEGAGALL RKQELVTQNE LLKQQVKIFE EDFQRERSDR 

       490        500        510        520        530        540 
ERMNEEKEEL KKQVEKLQAQ VTLSNAQLKA FKDEEKAREA LRQQKRKAKA SGERYHVEPH 

       550        560        570        580        590        600 
PEHLCGAYPY AYPPMPAMVP HHGFEDWSQI RYPPPPMAME HPPPLPNSRL FHLPEYTWRL 

       610        620        630 
PCGGVRNPNQ SSQVMDPPTA RPTEPESPKN DREGPQ 

« Hide

Isoform 2 (Beta) [UniParc].

Checksum: FE65D2CE6E7B185B
Show »

FASTA63571,788
Isoform 3 [UniParc].

Checksum: A97F0EB85F9F39DE
Show »

FASTA58366,012

References

« Hide 'large scale' references
[1]"Identification and cloning of a novel cellular protein Naf1, Nef-associated factor 1, that increases cell surface CD4 expression."
Fukushi M., Dixon J., Kimura T., Tsurutani N., Dixon M.J., Yamamoto N.
FEBS Lett. 442:83-88(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
Tissue: Peripheral blood.
[2]"A human nuclear shuttling protein that interacts with human immunodeficiency virus type 1 matrix is packaged into virions."
Gupta K., Ott D., Hope T.J., Siliciano R.F., Boeke J.D.
J. Virol. 74:11811-11824(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Leukocyte.
[3]"Prediction of the coding sequences of unidentified human genes. III. The coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by analysis of cDNA clones from human cell line KG-1."
Nagase T., Miyajima N., Tanaka A., Sazuka T., Seki N., Sato S., Tabata S., Ishikawa K., Kawarabayasi Y., Kotani H., Nomura N.
DNA Res. 2:37-43(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Bone marrow.
[4]"Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION.
[5]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
[6]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Tissue: Colon endothelium.
[7]"The DNA sequence and comparative analysis of human chromosome 5."
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S. expand/collapse author list , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Lung.
[10]"Transcriptional map of the Treacher Collins candidate gene region."
Loftus S.K., Dixon J., Koprivnikar K., Dixon M.J., Wasmuth J.J.
Genome Res. 6:26-34(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 136-636 (ISOFORM 2).
Tissue: Craniofacial.
[11]Fukushi M., Kimura T., Yamamoto N.
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 94-412.
[12]"A new ERK2 binding protein, Naf1, attenuates the EGF/ERK2 nuclear signaling."
Zhang S., Fukushi M., Hashimoto S., Gao C., Huang L., Fukuyo Y., Nakajima T., Amagasa T., Enomoto S., Koike K., Miura O., Yamamoto N., Tsuchida N.
Biochem. Biophys. Res. Commun. 297:17-23(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH MAPK1.
[13]"ABIN-1 binds to NEMO/IKKgamma and co-operates with A20 in inhibiting NF-kappaB."
Mauro C., Pacifico F., Lavorgna A., Mellone S., Iannetti A., Acquaviva R., Formisano S., Vito P., Leonardi A.
J. Biol. Chem. 281:18482-18488(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH IKBKG AND TNFAIP3.
[14]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-403, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"P-selectin primes leukocyte integrin activation during inflammation."
Wang H.B., Wang J.T., Zhang L., Geng Z.H., Xu W.L., Xu T., Huo Y., Zhu X., Plow E.F., Chen M., Geng J.G.
Nat. Immunol. 8:882-892(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH SELPLG AND PIK3CD, PHOSPHORYLATION AT TYR-552, MUTAGENESIS OF TYR-552.
[16]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-403, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-438, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[19]"A bacterial E3 ubiquitin ligase IpaH9.8 targets NEMO/IKKgamma to dampen the host NF-kappaB-mediated inflammatory response."
Ashida H., Kim M., Schmidt-Supprian M., Ma A., Ogawa M., Sasakawa C.
Nat. Cell Biol. 12:66-73(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH SHIGELLA FLEXNERI IPAH9.8, MUTAGENESIS OF 476-GLU-ARG-477.
[20]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-403 AND SER-442, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[21]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]"Polyubiquitin binding to ABIN1 is required to prevent autoimmunity."
Nanda S.K., Venigalla R.K., Ordureau A., Patterson-Kane J.C., Powell D.W., Toth R., Arthur J.S., Cohen P.
J. Exp. Med. 208:1215-1228(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITIN-BINDING, MUTAGENESIS OF ASP-472.
[23]"A20, ABIN-1/2, and CARD11 mutations and their prognostic value in gastrointestinal diffuse large B-cell lymphoma."
Dong G., Chanudet E., Zeng N., Appert A., Chen Y.W., Au W.Y., Hamoudi R.A., Watkins A.J., Ye H., Liu H., Gao Z., Chuang S.S., Srivastava G., Du M.Q.
Clin. Cancer Res. 17:1440-1451(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS TRP-263; MET-286; THR-374 AND LYS-476.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ011895 mRNA. Translation: CAA09855.1.
AJ011896 mRNA. Translation: CAA09856.1.
AY012155 mRNA. Translation: AAG42154.1.
D30755 mRNA. Translation: BAA06416.2.
AK299975 mRNA. Translation: BAH13185.1.
BX640647 mRNA. Translation: CAE45793.1.
AC008641 Genomic DNA. No translation available.
CH471062 Genomic DNA. Translation: EAW61690.1.
BC012133 mRNA. Translation: AAH12133.1.
BC014008 mRNA. Translation: AAH14008.1.
U39403 mRNA. Translation: AAC99999.1.
U83844 mRNA. Translation: AAB41438.1. Frameshift.
RefSeqNP_001239315.1. NM_001252386.1.
NP_001239319.1. NM_001252390.1.
NP_001239320.1. NM_001252391.1.
NP_001239321.1. NM_001252392.1.
NP_001239322.1. NM_001252393.1.
NP_001245383.1. NM_001258454.1.
NP_006049.3. NM_006058.4.
UniGeneHs.355141.
Hs.731557.

3D structure databases

ProteinModelPortalQ15025.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115602. 37 interactions.
DIPDIP-27577N.
IntActQ15025. 30 interactions.
MINTMINT-200912.
STRING9606.ENSP00000317891.

PTM databases

PhosphoSiteQ15025.

Polymorphism databases

DMDM20138952.

Proteomic databases

PaxDbQ15025.
PRIDEQ15025.

Protocols and materials databases

DNASU10318.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000315050; ENSP00000317891; ENSG00000145901. [Q15025-1]
ENST00000389378; ENSP00000374029; ENSG00000145901. [Q15025-1]
ENST00000518977; ENSP00000430971; ENSG00000145901. [Q15025-2]
ENST00000520931; ENSP00000429891; ENSG00000145901. [Q15025-3]
ENST00000521591; ENSP00000430760; ENSG00000145901. [Q15025-1]
ENST00000522226; ENSP00000428187; ENSG00000145901. [Q15025-1]
ENST00000523338; ENSP00000428243; ENSG00000145901. [Q15025-2]
GeneID10318.
KEGGhsa:10318.
UCSCuc003ltg.4. human. [Q15025-1]

Organism-specific databases

CTD10318.
GeneCardsGC05M150409.
HGNCHGNC:16903. TNIP1.
HPAHPA037893.
HPA037894.
MIM607714. gene.
neXtProtNX_Q15025.
Orphanet536. Systemic lupus erythematosus.
PharmGKBPA128394573.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG120932.
HOGENOMHOG000253048.
HOVERGENHBG019072.
InParanoidQ15025.
OMAPNSRLFH.
OrthoDBEOG7SJD44.
PhylomeDBQ15025.
TreeFamTF351138.

Gene expression databases

ArrayExpressQ15025.
BgeeQ15025.
CleanExHS_NAF1.
HS_TNIP1.
GenevestigatorQ15025.

Family and domain databases

ProtoNetSearch...

Other

ChiTaRSTNIP1. human.
GeneWikiTNIP1.
GenomeRNAi10318.
NextBio35479913.
PROQ15025.
SOURCESearch...

Entry information

Entry nameTNIP1_HUMAN
AccessionPrimary (citable) accession number: Q15025
Secondary accession number(s): B7Z699 expand/collapse secondary AC list , O76008, Q6N077, Q96EL9, Q99833, Q9H1J3
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: August 1, 1999
Last modified: April 16, 2014
This is version 131 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM